Glu-Asp-Arg
[CAS# 175175-23-2]

Identification

• Classification: Biochemical >> Inhibitor >> Angiogenesis >> BTK inhibitor
• Name: Glu-Asp-Arg
• Synonyms: Pinealon acetate salt form; (4S)-4-amino-5-[[(2S)-3-carboxy-1-[[(1S)-1-carboxy-4-(diaminomethylideneamino)butyl]amino]-1-oxopropan-2-yl]amino]-5-oxopentanoic acid
• Protein Sequence: EDR
• Molecular Formula: C₁₅H₂₆N₆O₈
• Molecular Weight: 418.40
• CAS Registry Number: 175175-23-2
• SMILES: C(C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)N)CN=C(N)N

Properties

• Density: 1.6±0.1 g/cm³ Calc.^*
• Index of refraction: 1.648 (Calc.)^*

^* Calculated using Advanced Chemistry Development (ACD/Labs) Software.

Discovory and Applicatios

Glu-Asp-Arg is a short tripeptide composed of three proteinogenic amino acids: glutamic acid, aspartic acid, and arginine, linked in this specific N-terminal to C-terminal sequence. As with many defined oligopeptides, its recognition and characterization are closely connected to the broader development of peptide chemistry, protein sequencing, and biochemical analysis rather than to a single isolated discovery event. The identification of short peptide sequences such as Glu-Asp-Arg became possible during the mid-twentieth century with advances in protein hydrolysis, chromatographic separation, and stepwise degradation techniques, which allowed researchers to determine the primary structures of proteins and their constituent peptide fragments.

The emergence of Glu-Asp-Arg as a defined chemical entity is linked to analytical studies of proteins and biologically active peptides. During enzymatic or chemical cleavage of proteins, small peptide fragments were isolated and sequenced to reconstruct larger macromolecular structures. In this context, tripeptides containing acidic and basic residues, including Glu-Asp-Arg, were identified and catalogued as part of systematic efforts to understand amino acid sequences and structure–function relationships in proteins. The establishment of solid-phase peptide synthesis further enabled the deliberate preparation of short peptides with defined sequences, making Glu-Asp-Arg readily accessible as a synthetic compound for research use.

Applications of Glu-Asp-Arg arise primarily from its role as a model peptide and as a functional sequence motif in biochemical and biomedical research. Short peptides are widely used to study peptide bond formation, hydrolysis, and conformational behavior in aqueous environments. Because Glu-Asp-Arg contains two acidic side chains and one basic side chain, it provides a useful system for examining charge interactions, salt bridge formation, and pH-dependent properties in peptides. Such studies contribute to a deeper understanding of protein folding, stability, and interactions.

In biological research, Glu-Asp-Arg has been investigated as a minimal sequence motif that can mimic or represent segments of larger proteins. Short peptide motifs are often synthesized to probe enzyme specificity, receptor recognition, or antibody binding without the complexity of full-length proteins. Peptides like Glu-Asp-Arg have therefore been used in binding assays, enzymatic studies, and structure–activity relationship analyses. In protease research, defined tripeptides serve as substrates or competitive inhibitors to characterize catalytic preferences and reaction mechanisms.

Glu-Asp-Arg and related oligopeptides have also found application in analytical chemistry and biotechnology. Synthetic peptides are commonly employed as calibration standards in chromatographic and mass spectrometric methods. The well-defined molecular mass and composition of Glu-Asp-Arg make it suitable for validating peptide analysis techniques, including liquid chromatography and tandem mass spectrometry. In addition, short peptides are frequently used in studies of peptide transport, degradation, and metabolism, providing insight into how small peptide fragments are handled in biological systems.

Although Glu-Asp-Arg itself is not used as a therapeutic agent, research on short peptides has influenced drug discovery and design. Understanding how specific amino acid sequences interact with biological targets has guided the development of peptide-based drugs and peptidomimetics. In this broader context, Glu-Asp-Arg represents a class of simple, well-characterized peptides that support fundamental research underlying advances in biochemistry, molecular biology, and medicinal chemistry.

References

Merrifield RB (1963) Solid phase peptide synthesis. I. The synthesis of a tetrapeptide. Journal of the American Chemical Society 85 14 2149–2154. DOI: 10.1021/ja00897a025

Aebersold R, Mann M (2003) Mass spectrometry-based proteomics. Nature 422 6928 198–207. DOI: 10.1038/nature01511